Dystrophin function: calcium-related rather than mechanical

Tay, JohnS.H.; Low, P. S.; Lee, W.L.; Lai, Poh San; Gan, Guixiang

doi:10.1016/0140-6736(90)91056-g

Cited by 6 publications

(1 citation statement)

References 5 publications

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“…However, the hypothesis was not supported by the following results: (1) virtually no difference in tensile strength of plasma membrane was found when normal and dystrophic sarcolemmal vesicles 24 and myotubes 19 were compared; (2) dystrophin deficiency did not influence the susceptibility of muscle to contractile activity-induced damage; 30 and (3) dystrophin function is related to calcium levels rather than to mechanical factors. 17,40 Therefore, the cause of muscle degeneration and the mechanism of calcium accumulation in muscle fibers have not been elucidated. Our preliminary findings and the findings of others indicate that the intracellular Ca 2+ concentrations in resting mdx EDL fibers are the same as those of control mice.…”

Section: Discussionmentioning

confidence: 99%

Skeletal muscle fiber degeneration in mdx mice induced by electrical stimulation

et al. 1997

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Section: Discussionmentioning

confidence: 99%

Skeletal muscle fiber degeneration in mdx mice induced by electrical stimulation

et al. 1997

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Dystrophin and a dystrophin-related protein in intrafusal muscle fibers, and neuromuscular and myotendinous junctions

et al. 1992

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To determine whether or not and how dystrophin exists in neuromuscular junctions (NMJs) and myotendinous junctions (MTJs), we studied the mid-belly and peripheral portions of control and mdx muscles, immunohistochemically and immunoelectrophoretically, using six kinds of polyclonal antibodies, and an antibody against a dystrophin-related protein (DRP). In controls these regions and the polar region of intrafusal muscle fibers showed a rather clearer immunohistochemical dystrophin reaction than those of extrafusal muscle fibers with all antibodies used. In the muscles of mdx mice NMJs only showed a positive dystrophin reaction with the c-terminal antibody, that is, no reaction with the other five antibodies, and MTJs in mdx showed a positive reaction with the c-terminal antibody and a faint to negative reaction with the other five antibodies. In biopsied human muscles NMJs and MTJs also showed a clear reaction with all ten antibodies, i.e., six polyclonal and four monoclonal ones. Although an immunohistochemical DRP reaction was clearly seen at NMJs, only a faint or no reaction was seen on MTJs and on intrafusal muscle fibers in both mouse and human materials. Western blot analysis of control mouse muscle for dystrophin showed a clearer band for the peripheral portion, which contains many MTJs, than for the mid-belly portion. These data suggest that dystrophin really exists on MTJs, and that dystrophin and DRP exist on NMJs in mouse and human muscles.

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N‐terminal domain of dystrophin

1994

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Contro-versial experiments have been published on calmodulin binding of dystrophin. In this study, we used recombinant proteins and the techniques of affinity chromatography and ELISA to show that the N-terminal part of dystrophin binds calmodulin specifically in a calciumdependent manner. The calcium-dependent interaction of calmodulin and dystrophin does not directly regulate binding of actin to dystrophin, but may regulate dystrophin interactions with other associated proteins.

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Dystrophin function: calcium-related rather than mechanical

Cited by 6 publications

References 5 publications

Skeletal muscle fiber degeneration in mdx mice induced by electrical stimulation

Skeletal muscle fiber degeneration in mdx mice induced by electrical stimulation

Dystrophin and a dystrophin-related protein in intrafusal muscle fibers, and neuromuscular and myotendinous junctions

N‐terminal domain of dystrophin

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